1e66

STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE X AT 2.1A RESOLUTION
(see also AChE inhibitors and substrates (Part II))



Huprine X (HUPerzine A + tacRINE) is one of the most potent reversible AChE inhibitors. This synthetic hybrid consists of a carbobicyclic moiety resembling that of (-)-huperzine A (colored blueviolet) and the 4-aminoquinoline substructure of tacrine (colored magenta). Both compounds are known AChE inhibitors. (−)-Huperzine A and tacrine are partially overlapping each other at the TcAChE active site. TcAChE residues interacting with (−)-huperzine A (1vot) are colored orange and with tacrine (1acj) in cyan. The conformation of 4-aminoquinoline substructure of huprine X in its complex with TcAChE (its interacting residues are in lime ) is very similar to those in the tacrine-TcAChE complex (1acj). The ring system of (−)-huperzine A is rotated almost by 180° in comparison to that of huprine X.

About this Structure
1E66 is a 1 chain structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.

Reference
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